| Type: | Family | Name: | Subtilin biosynthesis protein SpaC |
| Description: | The LanC-like protein superfamily encompasses a highly divergent group of peptide-modifying enzymes, including the eukaryotic and bacterial lanthionine synthetase C-like proteins (LanC) [, , ]; subtilin biosynthesis protein SpaC from Bacillus subtilis [, ]; epidermin biosynthesis protein EpiC from Staphylococcus epidermidis[]; nisin biosynthesis protein NisC from Lactococcus lactis[, , ]; GCR2 from Arabidopsis thaliana[]; and many others. The 3D structure of the lantibiotic cyclase from L. lactis has been determined by X-ray crystallography to 2.5A resolution []. The globular structure is characterised by an all-alpha fold, in which an outer ring of helices envelops an inner toroid composed of 7 shorter, hydrophobic helices. This 7-fold hyrophobic periodicity has led several authors to claim various members of the family, including eukaryotic LanC-1 and GCR2, to be novel G protein-coupled receptors [, ]; some of these claims have since been corrected [, , ]. The SpacC protein from B. subtilis is a cyclase enzyme involved in the biosynthesis of the lantibiotic subtilin [, , ].The protein exists as a monomer in solution and contains a stoichiometric zinc atom [], two cysteines and two histidines possibly acting as ligands to the metal; these cysteine residues are highly conserved in LanC-like proteins. | Short Name: | Subtilin_biosynthesis_SpaC |
